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AB171587

Recombinant Human RNF7 protein (denatured)

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Recombinant Human RNF7 protein (denatured) is a Human Full Length protein, in the 1 to 113 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE.

View Alternative Names

RBX2, ROC2, SAG, RNF7, RING-box protein 2, Rbx2, CKII beta-binding protein 1, RING finger protein 7, Regulator of cullins 2, Sensitive to apoptosis gene protein, CKBBP1

1 Images
SDS-PAGE - Recombinant Human RNF7 protein (denatured) (AB171587)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human RNF7 protein (denatured) (AB171587)

15% SDS-PAGE analysis of ab171587 at (3μg).

Key facts

Purity

>90% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

SDS-PAGE

applications

Biologically active

No

Accession

Q9UBF6

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 10% Glycerol (glycerin, glycerine), 2.4% Urea, 0.32% Tris HCl

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"MGSSHHHHHHSSGLVPRGSHMGSMADVEDGEETCALASHSGSSGSKSGGDKMFSLKKWNAVAMWSWDVECDTCAICRVQVMDACLRCQAENKQEDCVVVWGECNHSFHNCCMSLWVKQNNRCPLCQQDWVVQRIGK","proteinLength":"Full Length","predictedMolecularWeight":"15.1 kDa","actualMolecularWeight":null,"aminoAcidEnd":113,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"Q9UBF6","tags":[{"tag":"His","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False

Specifications

Form

Liquid

General info

Function

Catalytic component of multiple cullin-5-RING E3 ubiquitin-protein ligase complexes (ECS complexes), which mediate the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed : 21980433, PubMed : 33268465, PubMed : 38418882, PubMed : 38574733). It is thereby involved in various biological processes, such as cell cycle progression, signal transduction and transcription (PubMed : 21980433, PubMed : 33268465, PubMed : 38418882, PubMed : 38574733). The functional specificity of the E3 ubiquitin-protein ligase ECS complexes depend on the variable SOCS box-containing substrate recognition component (PubMed : 21980433, PubMed : 33268465). Within ECS complexes, RNF7/RBX2 recruits the E2 ubiquitination enzyme to the complex via its RING-type and brings it into close proximity to the substrate (PubMed : 34518685). Catalytic subunit of various SOCS-containing ECS complexes, such as the ECS(SOCS7) complex, that regulate reelin signaling by mediating ubiquitination and degradation of DAB1 (By similarity). The ECS(SOCS2) complex mediates the ubiquitination and subsequent proteasomal degradation of phosphorylated EPOR and GHR (PubMed : 21980433, PubMed : 25505247). Promotes ubiquitination and degradation of NF1, thereby regulating Ras protein signal transduction (By similarity). As part of the ECS(ASB9) complex, catalyzes ubiquitination and degradation of CKB (PubMed : 33268465). The ECS(SPSB3) complex catalyzes ubiquitination of nuclear CGAS (PubMed : 38418882). As part of some ECS complex, catalyzes 'Lys-11'-linked ubiquitination and degradation of BTRC (PubMed : 27910872). ECS complexes and ARIH2 collaborate in tandem to mediate ubiquitination of target proteins; ARIH2 mediating addition of the first ubiquitin on CRLs targets (PubMed : 34518685, PubMed : 38418882). Specifically catalyzes the neddylation of CUL5 via its interaction with UBE2F (PubMed : 19250909). Does not catalyze neddylation of other cullins (CUL1, CUL2, CUL3, CUL4A or CUL4B) (PubMed : 19250909). May play a role in protecting cells from apoptosis induced by redox agents (PubMed : 10082581).. Isoform 2. Inactive.. (Microbial infection) Following infection by HIV-1 virus, catalytic component of a cullin-5-RING E3 ubiquitin-protein ligase complex (ECS complex) hijacked by the HIV-1 Vif protein, which catalyzes ubiquitination and degradation of APOBEC3F and APOBEC3G.

Sequence similarities

Belongs to the RING-box family.

Post-translational modifications

Phosphorylation at Thr-10 by CK2 promotes its degradation by the proteasome.

Subcellular localisation

Nucleus

Product protocols

Target data

Catalytic component of multiple cullin-5-RING E3 ubiquitin-protein ligase complexes (ECS complexes), which mediate the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed : 21980433, PubMed : 33268465, PubMed : 38418882, PubMed : 38574733). It is thereby involved in various biological processes, such as cell cycle progression, signal transduction and transcription (PubMed : 21980433, PubMed : 33268465, PubMed : 38418882, PubMed : 38574733). The functional specificity of the E3 ubiquitin-protein ligase ECS complexes depend on the variable SOCS box-containing substrate recognition component (PubMed : 21980433, PubMed : 33268465). Within ECS complexes, RNF7/RBX2 recruits the E2 ubiquitination enzyme to the complex via its RING-type and brings it into close proximity to the substrate (PubMed : 34518685). Catalytic subunit of various SOCS-containing ECS complexes, such as the ECS(SOCS7) complex, that regulate reelin signaling by mediating ubiquitination and degradation of DAB1 (By similarity). The ECS(SOCS2) complex mediates the ubiquitination and subsequent proteasomal degradation of phosphorylated EPOR and GHR (PubMed : 21980433, PubMed : 25505247). Promotes ubiquitination and degradation of NF1, thereby regulating Ras protein signal transduction (By similarity). As part of the ECS(ASB9) complex, catalyzes ubiquitination and degradation of CKB (PubMed : 33268465). The ECS(SPSB3) complex catalyzes ubiquitination of nuclear CGAS (PubMed : 38418882). As part of some ECS complex, catalyzes 'Lys-11'-linked ubiquitination and degradation of BTRC (PubMed : 27910872). ECS complexes and ARIH2 collaborate in tandem to mediate ubiquitination of target proteins; ARIH2 mediating addition of the first ubiquitin on CRLs targets (PubMed : 34518685, PubMed : 38418882). Specifically catalyzes the neddylation of CUL5 via its interaction with UBE2F (PubMed : 19250909). Does not catalyze neddylation of other cullins (CUL1, CUL2, CUL3, CUL4A or CUL4B) (PubMed : 19250909). May play a role in protecting cells from apoptosis induced by redox agents (PubMed : 10082581).. Isoform 2. Inactive.. (Microbial infection) Following infection by HIV-1 virus, catalytic component of a cullin-5-RING E3 ubiquitin-protein ligase complex (ECS complex) hijacked by the HIV-1 Vif protein, which catalyzes ubiquitination and degradation of APOBEC3F and APOBEC3G.
See full target information RNF7

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